Madry, Christian ; Mesic, Ivana ; Bartholomäus, Ingo ; Nicke, Annette ; Betz, Heinrich ; Laube, Bodo (2007)
Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function.
In: Biochemical and biophysical research communications, 354 (1)
Article, Bibliographie
Abstract
Calcium-permeable N-methyl-d-aspartate (NMDA) receptors are tetrameric cation channels composed of glycine-binding NR1 and glutamate-binding NR2 subunits, which require binding of both glutamate and glycine for efficient channel gating. In contrast, receptors assembled from NR1 and NR3 subunits function as calcium-impermeable excitatory glycine receptors that respond to agonist application only with low efficacy. Here, we show that antagonists of and substitutions within the glycine-binding site of NR1 potentiate NR1/NR3 receptor function up to 25-fold, but inhibition or mutation of the NR3 glycine binding site reduces or abolishes receptor activation. Thus, glycine bound to the NR1 subunit causes auto-inhibition of NR1/NR3 receptors whereas glycine binding to the NR3 subunits is required for opening of the ion channel. Our results establish differential roles of the high-affinity NR3 and low-affinity NR1 glycine-binding sites in excitatory glycine receptor function.
| Item Type: | Article |
|---|---|
| Erschienen: | 2007 |
| Creators: | Madry, Christian ; Mesic, Ivana ; Bartholomäus, Ingo ; Nicke, Annette ; Betz, Heinrich ; Laube, Bodo |
| Type of entry: | Bibliographie |
| Title: | Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function. |
| Language: | English |
| Date: | 2007 |
| Journal or Publication Title: | Biochemical and biophysical research communications |
| Volume of the journal: | 354 |
| Issue Number: | 1 |
| Abstract: | Calcium-permeable N-methyl-d-aspartate (NMDA) receptors are tetrameric cation channels composed of glycine-binding NR1 and glutamate-binding NR2 subunits, which require binding of both glutamate and glycine for efficient channel gating. In contrast, receptors assembled from NR1 and NR3 subunits function as calcium-impermeable excitatory glycine receptors that respond to agonist application only with low efficacy. Here, we show that antagonists of and substitutions within the glycine-binding site of NR1 potentiate NR1/NR3 receptor function up to 25-fold, but inhibition or mutation of the NR3 glycine binding site reduces or abolishes receptor activation. Thus, glycine bound to the NR1 subunit causes auto-inhibition of NR1/NR3 receptors whereas glycine binding to the NR3 subunits is required for opening of the ion channel. Our results establish differential roles of the high-affinity NR3 and low-affinity NR1 glycine-binding sites in excitatory glycine receptor function. |
| Divisions: | 10 Department of Biology 10 Department of Biology > Neurophysiology and Neurosensory Systems ?? fb10_zoologie ?? |
| Date Deposited: | 11 Apr 2011 09:26 |
| Last Modified: | 05 Mar 2019 06:48 |
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